2W52
2 beta-glucans (6-O-glucosyl-laminaritriose) in both donor and acceptor sites of GH16 Laminarinase 16A from Phanerochaete chrysosporium.
Summary for 2W52
| Entry DOI | 10.2210/pdb2w52/pdb |
| Related | 2CL2 2W39 |
| Descriptor | PUTATIVE LAMINARINASE, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-glucopyranose-(1-6)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | laminarin, family 16, extracellular, beta sandwich, basidiomycete, beta- glucanase, glycosyl hydrolase, 3/1, gh7, gh16, lam16a, beta-1\, 6-glucan, hydrolase |
| Biological source | PHANEROCHAETE CHRYSOSPORIUM (WHITE-ROT FUNGUS) |
| Total number of polymer chains | 1 |
| Total formula weight | 34328.84 |
| Authors | Vasur, J.,Kawai, R.,Andersson, E.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J. (deposition date: 2008-12-03, release date: 2009-07-21, Last modification date: 2024-10-23) |
| Primary citation | Vasur, J.,Kawai, R.,Andersson, E.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J. X-Ray Crystal Structures of Phanerochaete Chrysosporium Laminarinase 16A in Complex with Products from Lichenin and Laminarin Hydrolysis FEBS J., 276:3858-, 2009 Cited by PubMed Abstract: The 1,3(4)-beta-D-glucanases of glycoside hydrolase family 16 provide useful examples of versatile yet specific protein-carbohydrate interactions. In the present study, we report the X-ray structures of the 1,3(4)-beta-D-glucanase Phanerochaete chrysosporium Laminarinase 16A in complex with beta-glucan products from laminarin (1.6 A) and lichenin (1.1 A) hydrolysis. The G6G3G3G glucan, in complex with the enzyme, showed a beta-1,6 branch in the acceptor site. The G4G3G ligand-protein complex showed that there was no room for a beta-1,6 branch in the -1 or -2 subsites; furthermore, the distorted residue in the -1 subsite and the glucose in the -2 subsite required a beta-1,3 bond between them. These are the first X-ray crystal structures of any 1,3(4)-beta-D-glucanase in complex with glucan products. They provide details of both substrate and product binding in support of earlier enzymatic evidence. PubMed: 19769746DOI: 10.1111/J.1742-4658.2009.07099.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
Download full validation report
